scholarly journals Septin pairs, a complex choreography

2011 ◽  
Vol 193 (6) ◽  
pp. 959-961 ◽  
Author(s):  
Helge Ewers

Septins form a filamentous collar at the mother–bud neck in budding yeast. In cytokinesis, this collar splits into two rings and the septin complexes undergo a dramatic reorientation. Using fluorescence polarization microscopy, DeMay et al. (2011. J. Cell Biol. doi:10.1083/jcb.201012143) now demonstrate that septin complexes assemble as paired filaments in vivo and reveal new insights into septin organization during cytokinesis.

Microscopy ◽  
2019 ◽  
Vol 68 (5) ◽  
pp. 359-368 ◽  
Author(s):  
Nori Nakai ◽  
Keisuke Sato ◽  
Tomomi Tani ◽  
Kenta Saito ◽  
Fumiya Sato ◽  
...  

Abstract Fluorescence polarization microscopy, which can visualize both position and orientation of fluorescent molecules, is useful for analyzing architectural dynamics of proteins in vivo, especially that of cytoskeletal proteins such as actin. Fluorescent phalloidin conjugates and SiR-actin can be used as F-actin orientation probes for fluorescence polarization microscopy, but a lack of appropriate methods for their introduction to living specimens especially to tissues, embryos, and whole animals hampers their applications to image the orientation of F-actin. To solve this problem, we have developed genetically encoded F-actin orientation probes for fluorescence polarization microscopy. We rigidly connected circular permutated green fluorescent protein (GFP) to the N-terminal α-helix of actin-binding protein Lifeact or utrophin calponin homology domain (UtrCH), and normal mEGFP to the C-terminal α-helix of UtrCH. After evaluation of ensemble and single particle fluorescence polarization with the instantaneous FluoPolScope, one of the constructs turned out to be suitable for practical usage in live cell imaging. Our new, genetically encoded F-actin orientation probe, which has a similar property of an F-actin probe to conventional GFP-UtrCH, is expected to report the 3D architecture of the actin cytoskeleton with fluorescence polarization microscopy, paving the way for both the single molecular orientation imaging in cultured cells and the sub-optical resolution architectural analysis of F-actin networks analysis of F-actin in various living systems.


2020 ◽  
Vol 118 (3) ◽  
pp. 308a-309a
Author(s):  
William F. Dean ◽  
Emily I. Bartle ◽  
Alexa L. Mattheyses

2017 ◽  
Vol 112 (3) ◽  
pp. 169a
Author(s):  
Emil Marklund ◽  
Elias Amselem ◽  
Kalle Kipper ◽  
Magnus Johansson ◽  
Sebastian Deindl ◽  
...  

ACS Nano ◽  
2016 ◽  
Vol 10 (3) ◽  
pp. 3873-3873
Author(s):  
Stefan Krause ◽  
Martin Neumann ◽  
Melanie Fröbe ◽  
Robert Magerle ◽  
Christian von Borczyskowski

2017 ◽  
Vol 11 (01) ◽  
pp. 1730002 ◽  
Author(s):  
Karl Zhanghao ◽  
Juntao Gao ◽  
Dayong Jin ◽  
Xuedian Zhang ◽  
Peng Xi

Fluorescence polarization is related to the dipole orientation of chromophores, making fluorescence polarization microscopy possible to reveal structures and functions of tagged cellular organelles and biological macromolecules. Several recent super resolution techniques have been applied to fluorescence polarization microscopy, achieving dipole measurement at nanoscale. In this review, we summarize both diffraction limited and super resolution fluorescence polarization microscopy techniques, as well as their applications in biological imaging.


Sign in / Sign up

Export Citation Format

Share Document